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Core2 beta-1,6-N-acetylglucosaminyltransferase enzyme activity is critical
for P-selectin glycoprotein ligand-1 binding to P-selectin
R Kumar, RT Camphausen, FX Sullivan and DA Cumming
Small Molecule Drug Discovery, Genetics Institute, Cambridge, MA 02140,
USA.
P-selectin glycoprotein ligand-1 (PSGL-1) is a high-affinity
counterreceptor for P-selectin on myeloid cells and activated T-cells. In
addition, PSGL-1 can serve, both in vitro and in vivo, as an E- selectin
ligand. Appropriate glycosylation of PSGL-1 is crucial for binding to
P-selectin. Functional PSGL-1 is known to bear sialyl lewis X (SLex) or a
closely related oligosaccharide. In this study, we show that Chinese
hamster ovary (CHO) cells expressing PSGL-1 and fucosyltransferase show a
dramatic increase in binding to P-selectin when transfected with "core2"
transferase, the enzyme that initiates branching of O-linked glycans.
Moreover, only PSGL-1 from core2 transfectant CHO cells can be
affinity-captured with P-selectin, suggesting that branched O-linked
glycans are required for high- affinity binding to P-selectin. Analysis of
PSGL-1-derived O-linked oligosaccharides produced in core2 transfected
cells shows the presence of more elaborated glycans. Interestingly,
transfection of core2 in these cells does not alter binding to E-selectin.
Volume 88,
Issue 10,
pp. 3872-3879,
11/15/1996
Copyright © 1996 by The American Society of Hematology
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